PHLD_MOUSE
ID PHLD_MOUSE Reviewed; 837 AA.
AC O70362;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
DE Short=PI-G PLD;
DE EC=3.1.4.50;
DE AltName: Full=Glycoprotein phospholipase D;
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D;
DE Short=GPI-PLD;
DE Short=GPI-specific phospholipase D;
DE Flags: Precursor;
GN Name=Gpld1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Glucagonoma;
RX PubMed=9716655; DOI=10.1007/s003359900851;
RA LeBoeuf R.C., Caldwell M., Guo Y., Metz C., Davitz M.A., Olson L.K.,
RA Deeg M.A.;
RT "Mouse glycosylphosphatidylinositol-specific phospholipase D (Gpld1)
RT characterization.";
RL Mamm. Genome 9:710-714(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-655.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-496.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This protein hydrolyzes the inositol phosphate linkage in
CC proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus
CC releasing these proteins from the membrane.
CC {ECO:0000269|PubMed:9716655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a
CC 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Associated with the High-Density
CC Lipoproteins (HDL). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9716655}.
CC -!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
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DR EMBL; AF050666; AAC77799.1; -; mRNA.
DR AlphaFoldDB; O70362; -.
DR STRING; 10090.ENSMUSP00000021773; -.
DR GlyConnect; 755; 2 N-Linked glycans (4 sites).
DR GlyGen; O70362; 10 sites, 3 N-linked glycans (4 sites).
DR iPTMnet; O70362; -.
DR PhosphoSitePlus; O70362; -.
DR SwissPalm; O70362; -.
DR CPTAC; non-CPTAC-3523; -.
DR CPTAC; non-CPTAC-3665; -.
DR jPOST; O70362; -.
DR MaxQB; O70362; -.
DR PaxDb; O70362; -.
DR PeptideAtlas; O70362; -.
DR PRIDE; O70362; -.
DR ProteomicsDB; 301814; -.
DR MGI; MGI:106604; Gpld1.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; O70362; -.
DR BRENDA; 3.1.4.50; 3474.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR ChiTaRS; Gpld1; mouse.
DR PRO; PR:O70362; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70362; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IDA:UniProtKB.
DR GO; GO:0004630; F:phospholipase D activity; IDA:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; ISS:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0071282; P:cellular response to iron(II) ion; ISO:MGI.
DR GO; GO:0071467; P:cellular response to pH; ISS:UniProtKB.
DR GO; GO:0071401; P:cellular response to triglyceride; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:UniProtKB.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IEP:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; IMP:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR GO; GO:0070633; P:transepithelial transport; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 3.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001028; Gprt_PLipase_D.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR029002; PLPC/GPLD1.
DR Pfam; PF01839; FG-GAP; 4.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00718; PHPHLIPASED.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
PE 1: Evidence at protein level;
KW Glycoprotein; HDL; Hydrolase; Lipid metabolism; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..837
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /id="PRO_0000022054"
FT REPEAT 364..425
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 431..492
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 494..554
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 561..619
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 629..689
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 701..767
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 785..837
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
SQ SEQUENCE 837 AA; 93255 MW; 9D007F479556CCC1 CRC64;
MSAGRLWSSL LLLLPLFCSK SSSCGLSTHV EIGHRALEFL RLQDGRINYK ELILEHQDAY
QAGTVFPDAF YPSICKRGKY HDVSERTHWT PFLNASIHYI RENYPLPWEK DTEKLVAFLF
GITSHMVADL SWHNLGFLRT MGAIDFYNSY SDAHSAGDFG GDVLSQFEFN FNYLSRRWYV
PVRDLLRIYD NLYGRKVITK DVLVDCTYLQ FLEMHGEMFA VSKLYSTYST KSPFLVEQFQ
DYFLGGLDDM AFWSTNIYRL TSFMLENGTS DCNLPENPLF ISCDGRNHTL SGSKVQKNDF
HRNLTMFISR DIRKNLNYTE RGVFYSTGSW ARPESVTFMY QTLERNLRLM LAGSSQKNLN
HVSSPSASYT LSVPYARLGW VMTSADLNQD GHGDLVVGAP GYSHPGRFQI GRVYIIYGND
LGLPPIDLDL NKEGILEGFQ PSGRFGSALA VLDFNQDGLP DLAVGAPSVG SGQLTYNGSV
YVYYGSQQGR LSSSPNVTIS CKDTYCNLGW TLLATDADGD GRHDLVISSP FAPGGRKQKG
IVATFYSHPR RNDKELLTLE EADWKVNGEE DFSWFGYSLH GVTVANRSLL LIGSPTWKNV
SRMARSSHKK NQEEKSLGKV YGYFLPNRQS TITISGDKAM GKLGTSLSSG YVRVNGTLTQ
VLLVGAPTHD DVSKMAFLTM TLHQGGATRM YELAPEKTQP ALLSTFSGDR RFSRFGSVLH
LTDLDDDGLD EIIMAAPLRI TDVTSGLLGG EDGRVYIYNG MYTTLGDMTG KCKSWMTPCP
EEKAQYVLTS PEASSRFGSS LVSVRSKGRN QVVVAAGRSS WGARLSGALH VYSFSSD
